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4U7L

LRIG1 extracellular domain: Structure and Function Analysis

Summary for 4U7L
Entry DOI10.2210/pdb4u7l/pdb
Related4U7M
DescriptorLeucine-rich repeats and immunoglobulin-like domains protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsstem cell marker, egfr inhibition, signaling protein
Biological sourceHomo sapiens (Human)
Cellular locationCell membrane ; Single-pass type I membrane protein : Q96JA1
Total number of polymer chains1
Total formula weight51598.07
Authors
Xu, Y. (deposition date: 2014-07-31, release date: 2015-04-08, Last modification date: 2023-09-27)
Primary citationXu, Y.,Soo, P.,Walker, F.,Zhang, H.H.,Redpath, N.,Tan, C.W.,Nicola, N.A.,Adams, T.E.,Garrett, T.P.,Zhang, J.G.,Burgess, A.W.
LRIG1 Extracellular Domain: Structure and Function Analysis.
J.Mol.Biol., 427:1934-1948, 2015
Cited by
PubMed Abstract: We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. The two LRIG1 domains crystallised so that we have been able to determine the three-dimensional structures at 2.3Å resolution. We developed a three-dimensional structure for the LRIG1-ECD using homology modelling based on the LINGO-1 structure. The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric. We could not detect any binding of the LRIG1 domains or the LRIG1-LRR-1Ig fragment to the EGF receptor (EGFR), either in solution using biosensor analysis or when the EGFR was expressed on the cell surface. The FLAG-tagged LRIG1-LRR-1Ig fragment binds weakly to colon cancer cells regardless of the presence of EGFRs. Similarly, neither the soluble LRIG1-LRR nor the LRIG1-3Ig domains nor the full-length LRIG1 co-expressed in HEK293 cells inhibited ligand-stimulated activation of cell-surface EGFR.
PubMed: 25765764
DOI: 10.1016/j.jmb.2015.03.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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